Details
| Original language | English |
|---|---|
| Pages (from-to) | 326-333 |
| Number of pages | 8 |
| Journal | Planta |
| Volume | 201 |
| Issue number | 3 |
| Publication status | Published - Mar 1997 |
Abstract
The 23-kDa nuclear-encoded heat-shock protein (HSP) of Chenopodium rubrum L. is regulated by light at tile posttranslational level. Higher light intensities are more effective in inducing the accumulation of the mature protein under heat-shock conditions. Based on this and other properties the protein was considered to belong to the group of small chloroplastic HSPs. However, we have now obtained the following evidence that this 23-kDa HSP is localized in the mitochondria: (i) Immunogold-labelled protein was almost exclusively restricted to the mitochondria in electron microscope thin sections. (ii) rising purified, isolated mitochondria from potato tubers the in-vitro-synthesized translation product of 31 kDa was readily transported into mitochondria where it was processed to the 23-kDa product. (iii) The protein could be detected by Western blotting in a preparation of washed mitochondria of Chenopodium, while under the same conditions no signal could be obtained in a preparation of isolated chloroplasts. (iv) Finally, sequence comparison with the published sequences of mitochondrial proteins by Lenne et al. (1995, Biochem J 311:805 813)and LaFayette et al. (1996, Plant Mol Biol 31):159 169) showed clearly that the 23-kDa protein is considerably more similar to these two proteins than to the group of plastid small HSPs. From these data we infer that mitochondria are involved in the response of the plants to high light stress under heat-shock conditions.
Keywords
- Cell culture (plant), Chenopodium Heat-shock protein (mitochondria), Mitochondrion Protein transport (in vitro)
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Planta, Vol. 201, No. 3, 03.1997, p. 326-333.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The 23-kDa light-stress-regulated heat-shock protein of Chenopodium rubrum L. is located in the mitochondria
AU - Debel, Karsten
AU - Sierralta, Walter D.
AU - Braun, Hans-Peter
AU - Schmitz, Udo
AU - Kloppstech, Klaus
N1 - Funding information: We gratefully acknowledge the skilful and excellent technical help by Mrs. Ingrid Bonig during the experiments. This work was generously supported by the Deutsche Forschungsgemeinschaft, Bonn, Germany. It was also carried out as part of a collaboration between Dr. S. Gepstein, Haifa Israel, and K.K. with the help of a grant (Stiftung Volkswagenwerk, Hannover) which was provided by the Ministry of Science and Arts of the Government of Niedersachsen, Germany.
PY - 1997/3
Y1 - 1997/3
N2 - The 23-kDa nuclear-encoded heat-shock protein (HSP) of Chenopodium rubrum L. is regulated by light at tile posttranslational level. Higher light intensities are more effective in inducing the accumulation of the mature protein under heat-shock conditions. Based on this and other properties the protein was considered to belong to the group of small chloroplastic HSPs. However, we have now obtained the following evidence that this 23-kDa HSP is localized in the mitochondria: (i) Immunogold-labelled protein was almost exclusively restricted to the mitochondria in electron microscope thin sections. (ii) rising purified, isolated mitochondria from potato tubers the in-vitro-synthesized translation product of 31 kDa was readily transported into mitochondria where it was processed to the 23-kDa product. (iii) The protein could be detected by Western blotting in a preparation of washed mitochondria of Chenopodium, while under the same conditions no signal could be obtained in a preparation of isolated chloroplasts. (iv) Finally, sequence comparison with the published sequences of mitochondrial proteins by Lenne et al. (1995, Biochem J 311:805 813)and LaFayette et al. (1996, Plant Mol Biol 31):159 169) showed clearly that the 23-kDa protein is considerably more similar to these two proteins than to the group of plastid small HSPs. From these data we infer that mitochondria are involved in the response of the plants to high light stress under heat-shock conditions.
AB - The 23-kDa nuclear-encoded heat-shock protein (HSP) of Chenopodium rubrum L. is regulated by light at tile posttranslational level. Higher light intensities are more effective in inducing the accumulation of the mature protein under heat-shock conditions. Based on this and other properties the protein was considered to belong to the group of small chloroplastic HSPs. However, we have now obtained the following evidence that this 23-kDa HSP is localized in the mitochondria: (i) Immunogold-labelled protein was almost exclusively restricted to the mitochondria in electron microscope thin sections. (ii) rising purified, isolated mitochondria from potato tubers the in-vitro-synthesized translation product of 31 kDa was readily transported into mitochondria where it was processed to the 23-kDa product. (iii) The protein could be detected by Western blotting in a preparation of washed mitochondria of Chenopodium, while under the same conditions no signal could be obtained in a preparation of isolated chloroplasts. (iv) Finally, sequence comparison with the published sequences of mitochondrial proteins by Lenne et al. (1995, Biochem J 311:805 813)and LaFayette et al. (1996, Plant Mol Biol 31):159 169) showed clearly that the 23-kDa protein is considerably more similar to these two proteins than to the group of plastid small HSPs. From these data we infer that mitochondria are involved in the response of the plants to high light stress under heat-shock conditions.
KW - Cell culture (plant)
KW - Chenopodium Heat-shock protein (mitochondria)
KW - Mitochondrion Protein transport (in vitro)
UR - http://www.scopus.com/inward/record.url?scp=1842292085&partnerID=8YFLogxK
U2 - 10.1007/s004250050074
DO - 10.1007/s004250050074
M3 - Article
C2 - 9129338
AN - SCOPUS:1842292085
VL - 201
SP - 326
EP - 333
JO - Planta
JF - Planta
SN - 0032-0935
IS - 3
ER -